Christian Kollewe

Summary

Affiliation: University of Giessen
Country: Germany

Publications

  1. ncbi Characterization of Pellino2, a substrate of IRAK1 and IRAK4
    Astrid Strelow
    Tularik Inc, 1120 Veterans Boulevard, South San Francisco, CA 94080, USA
    FEBS Lett 547:157-61. 2003
  2. ncbi Sequential autophosphorylation steps in the interleukin-1 receptor-associated kinase-1 regulate its availability as an adapter in interleukin-1 signaling
    Christian Kollewe
    Department of Pharmacology, Hannover Medical School, D 30623 Hannover, Germany
    J Biol Chem 279:5227-36. 2004
  3. ncbi Threonine 66 in the death domain of IRAK-1 is critical for interaction with signaling molecules but is not a target site for autophosphorylation
    Detlef Neumann
    Deptartment of Pharmacology, Hannover Medical School, Hannover, Germany
    J Leukoc Biol 84:807-13. 2008
  4. ncbi The death domain of IRAK-1: an oligomerization domain mediating interactions with MyD88, Tollip, IRAK-1, and IRAK-4
    Detlef Neumann
    Department for Pharmacology, Hannover Medical School, Carl Neuberg Str 1, D 30623 Hannover, Germany
    Biochem Biophys Res Commun 354:1089-94. 2007

Collaborators

Detail Information

Publications4

  1. ncbi Characterization of Pellino2, a substrate of IRAK1 and IRAK4
    Astrid Strelow
    Tularik Inc, 1120 Veterans Boulevard, South San Francisco, CA 94080, USA
    FEBS Lett 547:157-61. 2003
    ..However, unlike Pellino1, Pellino2 does not seem to activate a specific transcription factor, but links TIR signaling to basic cellular processes...
  2. ncbi Sequential autophosphorylation steps in the interleukin-1 receptor-associated kinase-1 regulate its availability as an adapter in interleukin-1 signaling
    Christian Kollewe
    Department of Pharmacology, Hannover Medical School, D 30623 Hannover, Germany
    J Biol Chem 279:5227-36. 2004
    ..Thus, IRAK-1 regulates its own availability as an adapter molecule by sequential autophosphorylation...
  3. ncbi Threonine 66 in the death domain of IRAK-1 is critical for interaction with signaling molecules but is not a target site for autophosphorylation
    Detlef Neumann
    Deptartment of Pharmacology, Hannover Medical School, Hannover, Germany
    J Leukoc Biol 84:807-13. 2008
    ..Thereby, it ensures the transient manner of interactions between IRAK-1 and the other signaling molecules. This essential role, however, is not regulated by phosphorylation of T66 itself...
  4. ncbi The death domain of IRAK-1: an oligomerization domain mediating interactions with MyD88, Tollip, IRAK-1, and IRAK-4
    Detlef Neumann
    Department for Pharmacology, Hannover Medical School, Carl Neuberg Str 1, D 30623 Hannover, Germany
    Biochem Biophys Res Commun 354:1089-94. 2007
    ..Finally, mutation of IRAK-1 at T66 not only allowed stable binding to the signaling adapters, but also enhanced its signaling capacity...